Further characterization of galactosylhydroxylysyl glucosyltransferase from chick embryos. Amino acid composition and acceptor specificity

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Abstract
A modified purification procedure, consisting of affinity chromatographies on concanavalin A-agarose, collagen-agarose and UDP-glucose-derivative-agarose and 1 gel filtration, is reported for galactosylhydroxylysyl glucosyltransferase [EC 2.4.1.66]. The enzyme obtained is entirely pure when studied by sodium dodecyl sulfate/polyacrylamide-gel electrophoresis. The enzyme protein was rich in glutamic acid+glutamine, aspartic acid + asparagine, glycine and alanine. The enzyme catalyzed no significant glucose transfer to any of the glycoproteins tested, except for collagens. This included all the glycoproteins that have previously served as glucosyl acceptors for impure enzyme preparations, thus indicating a high degree of specificity of the enzyme for galactosylhydroxylysine. Galactosylsphingosine would act as a glucosyl acceptor, however. This compound has a close structural similarity to galactosylhydroxylsine in that they both have an unsubstituted amino group next to the hydroxy group to which the galactose is attached.

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